ID A4EEV9_9RHOB Unreviewed; 519 AA.
AC A4EEV9;
DT 17-APR-2007, integrated into UniProtKB/TrEMBL.
DT 17-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00018198, ECO:0000256|HAMAP-Rule:MF_01025};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973, ECO:0000256|HAMAP-Rule:MF_01025};
DE AltName: Full=Alpha-IPM synthase {ECO:0000256|ARBA:ARBA00029993, ECO:0000256|HAMAP-Rule:MF_01025};
DE AltName: Full=Alpha-isopropylmalate synthase {ECO:0000256|HAMAP-Rule:MF_01025};
GN Name=leuA {ECO:0000256|HAMAP-Rule:MF_01025};
GN ORFNames=RCCS2_06079 {ECO:0000313|EMBL:EBA13431.1};
OS Roseobacter sp. CCS2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=391593 {ECO:0000313|EMBL:EBA13431.1, ECO:0000313|Proteomes:UP000003535};
RN [1] {ECO:0000313|EMBL:EBA13431.1, ECO:0000313|Proteomes:UP000003535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCS2 {ECO:0000313|EMBL:EBA13431.1,
RC ECO:0000313|Proteomes:UP000003535};
RA Mary Ann M.A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-
CC hydroxy-4-methylpentanoate (2-isopropylmalate). {ECO:0000256|HAMAP-
CC Rule:MF_01025}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178,
CC ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01025};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01025};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4. {ECO:0000256|ARBA:ARBA00004689,
CC ECO:0000256|HAMAP-Rule:MF_01025}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01025}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000256|ARBA:ARBA00009396,
CC ECO:0000256|HAMAP-Rule:MF_01025}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EBA13431.1}.
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DR EMBL; AAYB01000001; EBA13431.1; -; Genomic_DNA.
DR RefSeq; WP_008231150.1; NZ_AAYB01000001.1.
DR AlphaFoldDB; A4EEV9; -.
DR eggNOG; COG0119; Bacteria.
DR OrthoDB; 9803573at2; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000003535; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd07940; DRE_TIM_IPMS; 1.
DR Gene3D; 1.10.238.260; -; 1.
DR Gene3D; 3.30.160.270; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_01025; LeuA_type1; 1.
DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR005671; LeuA_bact_synth.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR00973; leuA_bact; 1.
DR PANTHER; PTHR10277:SF9; 2-ISOPROPYLMALATE SYNTHASE 1, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF08502; LeuA_dimer; 1.
DR SMART; SM00917; LeuA_dimer; 1.
DR SUPFAM; SSF110921; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:EBA13431.1};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01025};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|HAMAP-Rule:MF_01025};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01025};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430, ECO:0000256|HAMAP-
KW Rule:MF_01025};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01025};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01025}.
FT DOMAIN 7..268
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT REGION 391..519
FT /note="Regulatory domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT BINDING 16
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT BINDING 203
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT BINDING 205
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT BINDING 239
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
SQ SEQUENCE 519 AA; 56392 MW; F1C2CCF298C5D3BE CRC64;
MTKSNEVLIF DTTLRDGEQS PGATMTHDEK LEIAEMLDDM GVDIIEAGFP IASEGDFQAV
SEIAKLAKSA TICGLSRANY KDIDRCWEAV KHAKSPRIHT FIGTSPLHRA IPNLDMDEMA
ERIHDTVTHA RNLCDNVQWS PMDATRTEWD YLCRVVEIAI KAGATTINIP DTVGYTAPIE
SADLIRNLIS TVPGADDVIF ATHCHNDLGM ATANSLAAVE GGARQIECTI NGLGERAGNT
ALEEVVMALK VRGDIMPYTT KIDTRKIMNI SRRVATVSGF AVQFNKAIVG KNAFAHESGI
HQDGMLKNRE TFEVMKPEDV GLAGTSLPLG KHSGRAALRA KLNELGFDLA DNQLNDVFVR
FKDLADRKKE VFDDDLMALV TQNDAEDDRL KLKSLRVVCG TDGPQKADMV MEVDGADVET
SATGDGPVDA TFNAVKAIFS HGARLQIYQV SAVTEGTDAQ ATVSVRMEEE GRIATGQSAD
TDTVVASAKA YINALNRLLV RREQSEPGYD VKGVSYKDV
//
